从军曹鱼（Rachycentron canadum）皮中提取的酸溶性和胃蛋白酶溶性胶原蛋白的结构和特性。

Structure and characteristics of acid and pepsin-solubilized collagens from the skin of cobia (Rachycentron canadum).

机构信息

College of Food Science & Technology, Guangdong Ocean University, Zhanjiang 524088, China.

出版信息

Food Chem. 2012 Dec 1;135(3):1975-84. doi: 10.1016/j.foodchem.2012.06.086. Epub 2012 Jun 30.

DOI:10.1016/j.foodchem.2012.06.086

Abstract

Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from the skin of cobia (Rachycentron canadum). The yields of ASC and PSC were 35.5% and 12.3%, respectively. Based on the protein patterns and carboxymethyl-cellulose chromatography, ASC and PSC were composed of α1α2α3 heterotrimers and were characterised as type I collagen with no disulfide bond. Their amounts of imino acids were 203 and 191 residues per 1000 residues, respectively. LC-MS/MS analysis demonstrated the high sequences similarities of ASC and PSC. Fourier transform infrared spectroscopy spectra showed that the amide I, II and III peaks of PSC were obtained at a lower wave number compared with ASC. The thermal denaturation temperatures of ASC and PSC, as measured by viscometry, were 34.62 and 33.97°C, respectively. The transition temperatures (T(max)) were 38.17 and 36.03°C, respectively, as determined by differential scanning calorimetry (DSC). Both collagens were soluble at acidic pH and below 2% (w/v) NaCl concentration.

摘要

酸溶性胶原蛋白 (ASC) 和胃蛋白酶溶性胶原蛋白 (PSC) 从军曹鱼 (Rachycentron canadum) 的皮中提取。ASC 和 PSC 的产率分别为 35.5%和 12.3%。基于蛋白质图谱和羧甲基纤维素层析，ASC 和 PSC 由 α1α2α3 异三聚体组成，且为无二硫键的 I 型胶原蛋白。它们的亚氨基酸含量分别为每 1000 个残基 203 和 191 个残基。LC-MS/MS 分析表明 ASC 和 PSC 具有高度的序列相似性。傅里叶变换红外光谱显示，PSC 的酰胺 I、II 和 III 峰的波数低于 ASC。通过粘度法测量的 ASC 和 PSC 的热变性温度分别为 34.62 和 33.97°C。通过差示扫描量热法 (DSC) 确定的转变温度 (T(max)) 分别为 38.17 和 36.03°C。两种胶原蛋白在酸性 pH 和低于 2%（w/v）NaCl 浓度下均可溶解。